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Structural, Conformational and Interactional Investigation of Proteins with Related Sequences and Multiple Structures

机译:具有相关序列和多重结构的蛋白质的结构,构象和相互作用研究

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Homologous proteins are special macromolecules with related primary sequences and multiple native structures and together with sequence-unrelated nonhomologous ones both constitute the protein amazing universe. Here is made a thorough sample selection, and employed quantitative predictions to analyze structures, conformations, steric and hydrophobic interactions and underlying molecular mechanisms in proteins via two coarse-grained (hydrophobic-polar, large-small) models. First, five empirical relations from nonhomologous samples are determined correlating large and hydrophobic residue sequences from primary to helix and β-sheet structures of functional conformations. When applied to homologous proteins, such empirical relations allow precisely surveying the interaction performance, identifying four types of molecular mechanisms, and computing the stability level in conformation ensembles. 1764 structural inspections capture essential features and furnish structural-interactional insights for homologous proteins, as well as suggest a fruitful way for better understanding conformational variability in biomolecular processes such as protein evolution, dynamics, folding and design.
机译:同源蛋白质是具有相关的一级序列和多个天然结构的特殊大分子,与与序列无关的非同源蛋白质一起构成了蛋白质惊人的宇宙。在这里进行了彻底的样品选择,并通过两个粗粒度(疏水性极性,大-小)模型,采用定量预测分析了蛋白质中的结构,构象,空间和疏水相互作用以及潜在的分子机理。首先,确定了来自非同源样品的五个经验关系,这些关系将功能构象的一级到螺旋和β-折叠结构的大的疏水残基序列关联起来。当应用于同源蛋白质时,这样的经验关系可以精确地调查相互作用性能,识别四种类型的分子机制,并计算构象集合的稳定性水平。 1764年的结构检查捕获了同源蛋白的基本特征并提供了结构相互作用的见解,并为更好地理解生物分子过程中的构象变异性(例如蛋白进化,动力学,折叠和设计)提供了有效的方法。

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